ID A0A1S3IGT7_LINUN Unreviewed; 372 AA.
AC A0A1S3IGT7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Resistance to inhibitors of cholinesterase protein 3 {ECO:0000313|RefSeq:XP_013396689.1};
GN Name=LOC106163595 {ECO:0000313|RefSeq:XP_013396689.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013396689.1};
RN [1] {ECO:0000313|RefSeq:XP_013396689.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013396689.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ric-3 family.
CC {ECO:0000256|ARBA:ARBA00008538}.
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DR RefSeq; XP_013396689.1; XM_013541235.2.
DR AlphaFoldDB; A0A1S3IGT7; -.
DR EnsemblMetazoa; g1782.t1; g1782.t1; g1782.
DR EnsemblMetazoa; XM_013541235.2; XP_013396689.1; LOC106163595.
DR GeneID; 106163595; -.
DR KEGG; lak:106163595; -.
DR InParanoid; A0A1S3IGT7; -.
DR OMA; VIIMCFA; -.
DR OrthoDB; 2969701at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR InterPro; IPR026160; Ric3.
DR InterPro; IPR032763; RIC3_N.
DR PANTHER; PTHR21723; RESISTANCE TO INHIBITORS OF CHOLINESTERASE PROTEIN 3 RIC3; 1.
DR PANTHER; PTHR21723:SF3; RIC3 ACETYLCHOLINE RECEPTOR CHAPERONE, ISOFORM C; 1.
DR Pfam; PF15361; RIC3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..202
FT /note="Resistance to inhibitors of cholinesterase protein 3
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15361"
FT REGION 223..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 42075 MW; 497AD59B2E77DDD9 CRC64;
MDAKSIAVIC IVVGCLVVVY PKIFHPMIKR ALGFGEKTNA DKLDKNGMPH APKMRPGPMS
DRHMMGGTPH PGMRAAAEMR KQAMETQGSG RGGMVTMMLP VYTIGIVIYL IYTLCKIFNK
DDSKSGGRKN NVWYTDKLKS FTEEDSDEVG DEDYAEYIRK KKRQRELDIM LNKADERKIS
DYEMLQLQEK LLETEAQMQR IVDAMKQVQG KMTTVGSETV AQMSQGAGDS GSTEQLSKNQ
ETDMCEPMAD KLEQKEENAL DQISAQGASF DQEEEDELSF ADMSHDRTNF SEELGIEDSL
TESDSESEDT EAEQDNNETY RKHQQSDENE ENEVEEILLP ENKSDDTRCD DESDGLHHLR
KRQARDLHAA ED
//
